Optimized oxidoreductases for medium and large scale industrial biotransformations
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126
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[ 2017 ]
Alcalde M When directed evolution met ancestral enzyme resurrection
Microbial Biotechnol., 10: 22-24
[ 2017 ]
Ayuso-Fernández I, Martínez AT, Ruiz-Dueñas FJ Experimental recreation of the evolution of lignin-degrading enzymes from the Jurassic to date
Biotechnol. Biofuels, 10: 67
[ 2017 ]
Carro J, Martínez A, Medina M, Martínez AT, Ferreira P Protein dynamics promote hydride tunnelling in substrate oxidation by aryl-alcohol oxidase
Phys. Chem. Chem. Phys., 19: 28666-28675
[ 2017 ]
González-Pérez D, Alcalde M The making of versatile peroxidase by directed evolution
Biocatalysis and Biotransformation, doi: 10.1080/10242422.2017.1363190
[ 2017 ]
Gygli G, Lucas F, Guallar V, van Berkel WJ The ins and outs of vanillyl alcohol oxidase: Identification of ligand migration paths
PLoS Comput. Biol., 13
[ 2017 ]
Martínez AT, Ruiz-Dueñas FJ, Camarero S, Serrano A, Linde D, Lund H, Vind J, Tovborg M, Herold-Majumdar OM, Hofrichter M, Liers C, Ullrich R, Scheibner K, Sannia G, Piscitelli A, Sener ME, Kılıç S, van Berkel WJ, Guallar V, et al. Oxidoreductases on their way to industrial biotransformations
Biotechnol. Adv., 35: 815-831
year2017
Protein dynamics promote hydride tunnelling in substrate oxidation by aryl-alcohol oxidase
Carro J, Martínez A, Medina M, Martínez AT, Ferreira P
Phys. Chem. Chem. Phys., 19: 28666-28675
The temperature dependence of hydride transfer from the substrate to the N5 of the FAD cofactor during the reductive half-reaction of Pleurotus eryngii aryl-alcohol oxidase (AAO) is assessed here. Kinetic isotope effects on both the pre-steady state reduction of the enzyme and its steady-state kinetics, with differently deuterated substrates, suggest an environmentally-coupled quantum-mechanical tunnelling process. Moreover, those kinetic data, along with the crystallographic structure of the enzyme in complex with a substrate analogue, indicate that AAO shows a pre-organized active site that would only require the approaching of the hydride donor and acceptor for the tunnelled transfer to take place. Modification of the enzyme’s active-site architecture by replacement of Tyr92, a residue establishing hydrophobic interactions with the substrate analogue in the crystal structure, in the Y92F, Y92L and Y92W variants resulted in different temperature dependence patterns that indicated a role of this residue in modulating the transfer reaction.
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[ industrialoxidoreductases ]. Optimized oxidoreductases for medium and large scale industrial biotransformations. This project has received funding from the European Union’s Seventh Framework Programme for research, technological development and demonstration under Grant Agreement nº: FP7-KBBE-2013-7-613549. © indox 2013. Developed by
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